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Production and Characterization of Human Monoclonal Antibody Recognizing the N-Terminal Residues of Pseudomonas aeruginosa Exotoxin A

Hiroshi Ohtsuka, Kazuhiko Horigome, Hiroshi Ochi, TOSHIAKI NISHIMOTO, Tsuneo Kozuki, M. Kato, Takao Okuda, Hiroshi Noguchi

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Abstract

Human cell lines producing monoclonal antibodies (MAbs) against Pseudomonas aeruginosa exotoxin A were established by EBV transformation followed by cell fusion. Monoclonal antibody FK-001, IgM (mu, kappa), was demonstrated to be specifically reactive with exotoxin A in ELISA and immunoblotting, by recognizing N-terminal 16 amino acid residues of exotoxin A as an epitope. This epitope region belongs to domain I which is required for the binding of exotoxin A to the receptor on target cells. FK-001 showed a partial neutralizing activity for cell toxicity caused by exotoxin A and appeared to be effective against exotoxin A-producing P. aeruginosa infection in mice. A line of evidence suggests that monoclonal antibody FK-001 neutralizes exotoxin A-induced cell toxicity by the interference of accessibility and/or binding of exotoxin A to animal cell receptors.

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What this paper is about

Human cell lines producing monoclonal antibodies (MAbs) against Pseudomonas aeruginosa exotoxin A were established by EBV transformation followed by cell fusion. Monoclonal antibody FK-001, IgM (mu, kappa), was demonstrated to be specifically reactive with exotoxin A in ELISA and immunoblotting, by recognizing N-terminal 16 amino acid residues of exotoxin A as an epitope. This epitope region belongs to domain I which is required for the binding of exotoxin A to the receptor on target cells. FK-001 showed a partial neutralizing activity for cell toxicity caused by exotoxin A and appeared to be effective against exotoxin A-producing P. aeruginosa infection in mice. A line of evidence suggests that monoclonal antibody FK-001 neutralizes exotoxin A-induced cell toxicity by the interference of accessibility and/or binding of exotoxin A to animal cell receptors.

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Available abstract

Human cell lines producing monoclonal antibodies (MAbs) against Pseudomonas aeruginosa exotoxin A were established by EBV transformation followed by cell fusion. Monoclonal antibody FK-001, IgM (mu, kappa), was demonstrated to be specifically reactive with exotoxin A in ELISA and immunoblotting, by recognizing N-terminal 16 amino acid residues of exotoxin A as an epitope. This epitope region belongs to domain I which is required for the binding of exotoxin A to the receptor on target cells. FK-001 showed a partial neutralizing activity for cell toxicity caused by exotoxin A and appeared to be effective against exotoxin A-producing P. aeruginosa infection in mice. A line of evidence suggests that monoclonal antibody FK-001 neutralizes exotoxin A-induced cell toxicity by the interference of accessibility and/or binding of exotoxin A to animal cell receptors.

Key concepts: Exotoxin, Pseudomonas exotoxin, Monoclonal antibody, Epitope, Biology, Molecular biology, Antibody, Microbiology

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Production and Characterization of Human Monoclonal Antibody Recognizing the N-Terminal Residues of Pseudomonas aeruginosa Exotoxin A — Research Paper | ScholarLens